title: Characterization of soluble artificial proteins with random sequences.
abstract: The structural and catalytic properties of two soluble random proteins, RP3-42 and RP3-45, of 141 amino acid residues were investigated. Although no marked secondary structure was detected by CD spectrum, sedimentation equilibrium and small-angle X-ray scattering studies showed that they form an oligomeric structure and are as compact as the molten globule. The random proteins have low but distinct esterase activity; the values of the second-order rate constant for the hydrolysis of p-nitrophenol were 0.78 and 1.39 M(-1) s(-1) for RP3-42 and RP3-45, respectively. The differences in the properties of the random and the native proteins are discussed from the evolutionary point of view.
authors.affiliation: Department of Biotechnology, Faculty of Engineering, Osaka University, Suita, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Yamauchi
authors.forename: T
authors.initials: T
authors.lastname: Yomo
authors.forename: F
authors.initials: F
authors.lastname: Tanaka
authors.forename: I D
authors.initials: ID
authors.lastname: Prijambada
authors.forename: S
authors.initials: S
authors.lastname: Ohhashi
authors.forename: K
authors.initials: K
authors.lastname: Yamamoto
authors.forename: Y
authors.initials: Y
authors.lastname: Shima
authors.forename: K
authors.initials: K
authors.lastname: Ogasahara
authors.forename: K
authors.initials: K
authors.lastname: Yutani
authors.forename: M
authors.initials: M
authors.lastname: Kataoka
authors.forename: I
authors.initials: I
authors.lastname: Urabe
mesh_terms: D000595:Amino Acid Sequence; D000645:Ammonium Sulfate; D002384:Catalysis; D011232:Chemical Precipitation; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D012995:Solubility
chemical_list: D009842:Oligopeptides; D011506:Proteins; D000645:Ammonium Sulfate